TDP-L-mycarose | 452322-67-7

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘧啶核苷酸
• 英文名称: TDP-L-mycarose
• 英文别名: dTDP-beta-L-mycarose；[(2R,4R,5S,6S)-4,5-dihydroxy-4,6-dimethyloxan-2-yl] [hydroxy-[[(2R,3S,5R)-3-hydroxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy]phosphoryl] hydrogen phosphate
• CAS: 452322-67-7
• 化学式: C₁₇H₂₈N₂O₁₄P₂
• 分子量: 546.362
• InChiKey: WILFWCJMOXHLEQ-ORWDRJNOSA-N

物化性质

• 密度：
  1.68±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -3.6
• 重原子数：
  35
• 可旋转键数：
  8
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.76
• 拓扑面积：
  231
• 氢给体数：
  6
• 氢受体数：
  14

反应信息

• 作为反应物：
  描述：

  TDP-L-mycarose 、 vicenilactam 在 Vin C from Escherichia coli pETvinC Tris-HCl buffer 作用下， 以 二甲基亚砜 为溶剂， 以40%的产率得到L-mycarose-α-vicenilactam
  参考文献：
  名称：

  Substrate Flexibility of Vicenisaminyltransferase VinC Involved in the Biosynthesis of Vicenistatin

  摘要：

  A glycosyltransferase VinC is involved in the biosynthesis of antitumor beta-glycoside antibiotic vicenistatin. It catalyzes a glycosyl transfer reaction between dTDP-alpha-D-vicenisamine and vicenilactam. Previous identification of its broad substrate specificity toward various glycosyl acceptors enabled us to explore the potential of VinC for glycodiversification. In vitro study of the substrate specificity toward several dTDP-sugars with vicenilactam established that VinC displayed activities with alpha-anomers of several dTDP-2-deoxy-D-sugars such as mycarose, digitoxose, olivose, and 2-deoxyglucose to afford respective beta-glycosides. Notably, beta-anomers of dTDP-2-deoxy-D-sugars also appeared to be accepted by VinC to form alpha-glycosides. Furthermore, VinC is capable of catalyzing glycosyl transfer reactions from both the alpha-anomer and beta-anomer of dTDP-L-mycarose, respectively, into beta-glycoside and alpha-glycoside. These results indicate that VinC is a unique glycosyltransferase possessing broad substrate specificity. The mechanism of this axially oriented glycosidic bond formation from the equatorially oriented dTDP-sugar might be explained by conformational change of dTDP-sugar to a boat conformation during the glycosyl transfer reaction. To apply these features of VinC for glycodiversification, 22 sets of structurally diverse glycosides were constructed using unnatural glycosyl donors and acceptors.

  DOI：

  10.1021/ja0685250
• 作为产物：
  描述：

  methyl α-L-mycaroside 在 溶剂黄146 作用下， 以 水 为溶剂， 生成 TDP-L-mycarose
  参考文献：
  名称：

  Substrate Flexibility of Vicenisaminyltransferase VinC Involved in the Biosynthesis of Vicenistatin

  摘要：

  A glycosyltransferase VinC is involved in the biosynthesis of antitumor beta-glycoside antibiotic vicenistatin. It catalyzes a glycosyl transfer reaction between dTDP-alpha-D-vicenisamine and vicenilactam. Previous identification of its broad substrate specificity toward various glycosyl acceptors enabled us to explore the potential of VinC for glycodiversification. In vitro study of the substrate specificity toward several dTDP-sugars with vicenilactam established that VinC displayed activities with alpha-anomers of several dTDP-2-deoxy-D-sugars such as mycarose, digitoxose, olivose, and 2-deoxyglucose to afford respective beta-glycosides. Notably, beta-anomers of dTDP-2-deoxy-D-sugars also appeared to be accepted by VinC to form alpha-glycosides. Furthermore, VinC is capable of catalyzing glycosyl transfer reactions from both the alpha-anomer and beta-anomer of dTDP-L-mycarose, respectively, into beta-glycoside and alpha-glycoside. These results indicate that VinC is a unique glycosyltransferase possessing broad substrate specificity. The mechanism of this axially oriented glycosidic bond formation from the equatorially oriented dTDP-sugar might be explained by conformational change of dTDP-sugar to a boat conformation during the glycosyl transfer reaction. To apply these features of VinC for glycodiversification, 22 sets of structurally diverse glycosides were constructed using unnatural glycosyl donors and acceptors.

  DOI：

  10.1021/ja0685250

文献信息

• A Two-Stage One-Pot Enzymatic Synthesis of TDP-<scp>l</scp>-mycarose from Thymidine and Glucose-1-phosphate
  作者：Haruko Takahashi、Yung-nan Liu、Hung-wen Liu

  DOI：10.1021/ja0562144

  日期：2006.2.1

  This report describes a procedure combining six enzymes native to Escherichia coli or Salmonella typhi, such as thymidine kinase (TK), thymidylate kinase (TMK), nucleoside diphosphate kinase (NDK), pyruvate kinase (PK; for ATP regeneration), TDP-glucose synthetase (RfbA), and TDP-glucose 4,6-dehydratase (RfbB), with five enzymes from Streptomyces fradiae, such as TylX3, TylC1, TylC3, TylK, and TylC2, that resulted in the biosynthesis of TDP-l-mycarose from glucose-1-phosphate and thymidine. This two-stage one-pot approach can be readily applied to the synthesis of other unusual sugars.